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Protein

Transcription factor E2F7

Gene

E2f7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation.8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi143 – 212Sequence analysisAdd BLAST70
DNA bindingi283 – 368Sequence analysisAdd BLAST86

GO - Molecular functioni

  • core promoter binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • chorionic trophoblast cell differentiation Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • hepatocyte differentiation Source: UniProtKB
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cytokinesis Source: UniProtKB
  • negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKB
  • placenta development Source: UniProtKB
  • positive regulation of DNA endoreduplication Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • sprouting angiogenesis Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • trophoblast giant cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Cell cycle, DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F7
Short name:
E2F-7
Gene namesi
Name:E2f7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1289147. E2f7.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype; mice develop normally and live to old age. E2f7 and E2f8 double knockout embryos die by 11.5 dpc of massive apoptosis and dilation of blood vessels and show increased expression of E2f1 and Tp53, as well as many stress-related genes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002989081 – 904Transcription factor E2F7Add BLAST904

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei96PhosphoserineBy similarity1
Modified residuei411PhosphoserineBy similarity1
Modified residuei833PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ6S7F2.
PRIDEiQ6S7F2.

PTM databases

iPTMnetiQ6S7F2.
PhosphoSitePlusiQ6S7F2.

Expressioni

Tissue specificityi

Widely expressed with highest levels in skin and thymus and very low levels in brain, muscle and stomach. Expressed in trophoblast giant cells throughout placenta development (at protein level).3 Publications

Developmental stagei

Highly expressed during mid to late S-phase.1 Publication

Inductioni

Induced at the onset of hepatocyte polyploidization.1 Publication

Gene expression databases

BgeeiENSMUSG00000020185.
CleanExiMM_E2F7.
ExpressionAtlasiQ6S7F2. baseline and differential.
GenevisibleiQ6S7F2. MM.

Interactioni

Subunit structurei

Interacts with HIF1A (By similarity). Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HIF1AQ166653EBI-8030813,EBI-447269From a different organism.

Protein-protein interaction databases

IntActiQ6S7F2. 1 interactor.
MINTiMINT-8410146.
STRINGi10090.ENSMUSP00000073453.

Structurei

3D structure databases

ProteinModelPortaliQ6S7F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer (PubMed:12893818).1 Publication

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ6S7F2.
KOiK09391.
OMAiSLVMPKK.
OrthoDBiEOG091G0F9Z.
PhylomeDBiQ6S7F2.
TreeFamiTF105567.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 3 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6S7F2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEVNCLTLKD LISPRQTRLD FAIEDAENAQ KENIFVDRSR MTPKTPMKNE
60 70 80 90 100
PIDLSKQRIF TPDRNPITPV KPVDRQPQVE PWTPTANLKM LISAASPDIR
110 120 130 140 150
DREKKKELFR PIENKEDAFV NSLQLDVAGD GAVDEYEKQR PSRKQKSLGL
160 170 180 190 200
LCQKFLARYP SYPLSTEKTT ISLDEVAVSL GVERRRIYDI VNVLESLHLV
210 220 230 240 250
SRVAKNQYGW HGRHSLPKTL RTLQRLGEEQ KYEEQMACLQ QKELDLMGYR
260 270 280 290 300
FGERRKDGSP DPRDPHLLDF SEADYPSSSA NSRKDKSLRI MSQKFVMLFL
310 320 330 340 350
VSKTKIVTLD VAAKILIEES QDTPDHSKFK TKVRRLYDIA NVLTSLALIK
360 370 380 390 400
KVHVTEERGR KPAFKWIGPV DFSSIDEELL DVSASILPEL KKEAYGQIRV
410 420 430 440 450
CAKERLVRYG SFNTVHTSEK IQRKVSSEPS SPQGERQGSA YSLEIGSLAA
460 470 480 490 500
IYRQKVEDNS QEEAFVSNTA VPPASILDPA LSMDSEYCVK PLAQPVFSVA
510 520 530 540 550
QTDLPAFSAQ NGPSGQVGVP VPSAASDTEN LKPALLAGQP LVYVPSTQLF
560 570 580 590 600
MLYGSVQEGL SPESRSEEDG GGSDVPADLS VTPSAQKRLC EERDPQEEED
610 620 630 640 650
EPAMKRQSQE FEDSPLSLVM PKKPSSSTDL ACPVTMGNGS SPPLEDACVK
660 670 680 690 700
GQLPAAEEVT GKAAPNCYVA SECGNPARNP DTEKPSNENE ITKDPSLMQY
710 720 730 740 750
LYVQSPAGLN GFNMVLPGTQ TPHTVAPSPA QLPSFGVPCM FLQSPGLGPF
760 770 780 790 800
PVLYSPAIPG PISSAPGTHP NPGPMNFGLS TLASASHLLI SPAAMVNPKP
810 820 830 840 850
STLPCTDPQL RCQPSLNLNP VMPGSHGVIH PESPCYVRHP VSMVKAEQSP
860 870 880 890 900
APATPKSIQR RHRETFFKTP GSLGDPVFRR KERNQSRNTS SAQRRLEISS

SGPD
Length:904
Mass (Da):99,535
Last modified:July 5, 2004 - v1
Checksum:i1EABCD1805FF80D2
GO
Isoform 2 (identifier: Q6S7F2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     376-421: DEELLDVSAS...FNTVHTSEKI → GKEMRSFDKD...LRLMTSLLEQ
     422-904: Missing.

Note: No experimental confirmation available.
Show »
Length:421
Mass (Da):48,660
Checksum:i37EC85E9E07F8469
GO

Sequence cautioni

The sequence BAC32193 differs from that shown. Reason: Frameshift at position 738.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73V → D in BAC27243 (PubMed:16141072).Curated1
Sequence conflicti159Y → H in BAC32193 (PubMed:16141072).Curated1
Sequence conflicti266H → L in AAI50773 (Ref. 3) Curated1
Sequence conflicti266H → L in AAI45430 (Ref. 3) Curated1
Sequence conflicti300L → H in BAC27243 (PubMed:16141072).Curated1
Sequence conflicti776N → D in BAC32193 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044618376 – 421DEELL…TSEKI → GKEMRSFDKDLWYIPFPSST CRQQNWPFPVLPVTRNLRLM TSLLEQ in isoform 2. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_044619422 – 904Missing in isoform 2. 1 PublicationAdd BLAST483

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY463359 mRNA. Translation: AAR26542.1.
AK031078 mRNA. Translation: BAC27243.1.
AK045040 mRNA. Translation: BAC32193.1. Frameshift.
AK041481 mRNA. Translation: BAC30958.1.
AK143686 mRNA. Translation: BAE25497.1.
CH466539 Genomic DNA. Translation: EDL21712.1.
BC145429 mRNA. Translation: AAI45430.1.
BC150772 mRNA. Translation: AAI50773.1.
CCDSiCCDS36055.1. [Q6S7F2-1]
RefSeqiNP_848724.2. NM_178609.4. [Q6S7F2-1]
XP_006513945.1. XM_006513882.3. [Q6S7F2-1]
UniGeneiMm.11747.

Genome annotation databases

EnsembliENSMUST00000073781; ENSMUSP00000073453; ENSMUSG00000020185. [Q6S7F2-1]
ENSMUST00000173471; ENSMUSP00000133494; ENSMUSG00000020185. [Q6S7F2-1]
GeneIDi52679.
KEGGimmu:52679.
UCSCiuc007gzo.1. mouse. [Q6S7F2-2]
uc007gzp.1. mouse. [Q6S7F2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY463359 mRNA. Translation: AAR26542.1.
AK031078 mRNA. Translation: BAC27243.1.
AK045040 mRNA. Translation: BAC32193.1. Frameshift.
AK041481 mRNA. Translation: BAC30958.1.
AK143686 mRNA. Translation: BAE25497.1.
CH466539 Genomic DNA. Translation: EDL21712.1.
BC145429 mRNA. Translation: AAI45430.1.
BC150772 mRNA. Translation: AAI50773.1.
CCDSiCCDS36055.1. [Q6S7F2-1]
RefSeqiNP_848724.2. NM_178609.4. [Q6S7F2-1]
XP_006513945.1. XM_006513882.3. [Q6S7F2-1]
UniGeneiMm.11747.

3D structure databases

ProteinModelPortaliQ6S7F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6S7F2. 1 interactor.
MINTiMINT-8410146.
STRINGi10090.ENSMUSP00000073453.

PTM databases

iPTMnetiQ6S7F2.
PhosphoSitePlusiQ6S7F2.

Proteomic databases

PaxDbiQ6S7F2.
PRIDEiQ6S7F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073781; ENSMUSP00000073453; ENSMUSG00000020185. [Q6S7F2-1]
ENSMUST00000173471; ENSMUSP00000133494; ENSMUSG00000020185. [Q6S7F2-1]
GeneIDi52679.
KEGGimmu:52679.
UCSCiuc007gzo.1. mouse. [Q6S7F2-2]
uc007gzp.1. mouse. [Q6S7F2-1]

Organism-specific databases

CTDi144455.
MGIiMGI:1289147. E2f7.

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ6S7F2.
KOiK09391.
OMAiSLVMPKK.
OrthoDBiEOG091G0F9Z.
PhylomeDBiQ6S7F2.
TreeFamiTF105567.

Miscellaneous databases

ChiTaRSiE2f7. mouse.
PROiQ6S7F2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020185.
CleanExiMM_E2F7.
ExpressionAtlasiQ6S7F2. baseline and differential.
GenevisibleiQ6S7F2. MM.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 3 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiE2F7_MOUSE
AccessioniPrimary (citable) accession number: Q6S7F2
Secondary accession number(s): B2RWZ8
, Q8BRE2, Q8BSQ3, Q8C9R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.